Structural basis for detoxification and oxidative stress protection in membranes

Forskningsoutput: TidskriftsbidragArtikel i vetenskaplig tidskrift

Abstract

Synthesis of mediators of fever, pain and inflammation as well as protection against reactive molecules and oxidative stress is a hallmark of the MAPEG superfamily (membrane associated proteins in eicosanoid and glutathione metabolism). The structure of a MAPEG member, rat mictosomal glutathione transferase 1, at 3.2 angstrom resolution, solved here in complex with glutathione by electron crystallography, defines the active site location and a cytosolic domain involved in enzyme activation. The glutathione binding site is found to be different from that of the canonical soluble glutathione transferases. The architecture of the homotrimer supports a catalytic mechanism involving subunit interactions and reveals both cytosolic and membraneous substrate entry sites, providing a rationale for the membrane location of the enzyme.

Detaljer

Författare
  • Peter Holm
  • Priyaranjan Bhakat
  • Caroline Jegerschold
  • Nobuhiko Gyobu
  • Kaoru Mitsuoka
  • Yoshinori Fujiyoshi
  • Ralf Morgenstern
  • Hans Hebert
Enheter & grupper
Forskningsområden

Ämnesklassifikation (UKÄ) – OBLIGATORISK

  • Biologiska vetenskaper

Nyckelord

Originalspråkengelska
Sidor (från-till)934-945
TidskriftJournal of Molecular Biology
Volym360
Utgåva nummer5
StatusPublished - 2006
PublikationskategoriForskning
Peer review utfördJa